| Autor: |
J. H. Bradbury, V. Ramesh |
| Rok vydání: |
2009 |
| Předmět: |
|
| Zdroj: |
International Journal of Peptide and Protein Research. 28:146-153 |
| ISSN: |
0367-8377 |
| DOI: |
10.1111/j.1399-3011.1986.tb03241.x |
| Popis: |
1H n.m.r. studies at 270 MHz were made of the transformation of 2 Zn insulin hexamer to 4 Zn hexamer produced by the addition of anions (thiocyanate ion). Four separate H2 histidine resonances were observed for the B5 and B10 histidines in 2 Zn hexamer at pH 7 and 9 and four separate resonances also occurred in the 4 Zn hexamer. The observation of these resonances and others from phenylalanine, tyrosine and leucine residues showed that the 2 Zn to 4 Zn transformation probably occurred in solution in a similar manner to that observed in the crystal. Furthermore as occurred in the crystal, it was found that in solution the transformation was reversible (on removal of thiocyanate) and that 2 Cd insulin was unable to undergo the transformation. Des-Phe-B1-insulin did not undergo the transformation. Addition of SCN˜ to Zn-free insulin (mainly dimer) produced only a small transformation, consistent with the idea that Zn2 + promotes formation of hexamer from dimer but probably does not otherwise affect the transformation. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
